Inhibiting HCMV pUL89-C Endonuclease with Metal-Binding Compounds: Miniperspective

AD Jagtap, RJ Geraghty, Z Wang - Journal of medicinal chemistry, 2023 - ACS Publications
Human cytomegalovirus (HCMV) infects individuals of all ages and establishes a lifelong
latency. Current antiviral drugs are suboptimal in efficacy and safety and ineffective against …

4, 5-Dihydroxypyrimidine methyl carboxylates, carboxylic acids, and carboxamides as inhibitors of human cytomegalovirus pUL89 endonuclease

T He, TC Edwards, J Xie, H Aihara… - Journal of medicinal …, 2022 - ACS Publications
Human cytomegalovirus (HCMV) terminase complex entails a metal-dependent
endonuclease at the C-terminus of pUL89 (pUL89-C). We report herein the design …

Metal binding 6-arylthio-3-hydroxypyrimidine-2, 4-diones inhibited human cytomegalovirus by targeting the pUL89 endonuclease of the terminase complex

L Wang, TC Edwards, RL Sahani, J Xie… - European journal of …, 2021 - Elsevier
The genome packaging of human cytomegalovirus (HCMV) requires a divalent metal-
dependent endonuclease activity localized to the C-terminus of pUL89 (pUL89-C), which is …

Metal-chelating 3-hydroxypyrimidine-2, 4-diones inhibit human cytomegalovirus pUL89 endonuclease activity and virus replication

Y Wang, J Tang, Z Wang, RJ Geraghty - Antiviral Research, 2018 - Elsevier
Human cytomegalovirus terminase complex cleaves the concatemeric genomic viral DNA
into unit lengths during genome packaging and particle assembly. Terminase complex …

Hydroxypyridonecarboxylic acids as inhibitors of human cytomegalovirus pUL89 endonuclease

J Kankanala, Y Wang, RJ Geraghty, Z Wang - ChemMedChem, 2018 - Wiley Online Library
Human cytomegalovirus (HCMV) infection poses a major health threat to
immunocompromised individuals. Until recently, treatment of HCMV infection has relied …

Repurposing N-hydroxy thienopyrimidine-2, 4-diones (HtPD) as inhibitors of human cytomegalovirus pUL89 endonuclease: Synthesis and biological characterization

T He, TC Edwards, R Majima, E Jung, J Kankanala… - Bioorganic …, 2022 - Elsevier
The terminase complex of human cytomegalovirus (HCMV) is required for viral genome
packaging and cleavage. Critical to the terminase functions is a metal-dependent …

8‐Hydroxy‐1, 6‐naphthyridine‐7‐carboxamides as Inhibitors of Human Cytomegalovirus pUL89 Endonuclease

E Jung, R Majima, TC Edwards, R Soto‐Acosta… - …, 2022 - Wiley Online Library
Human cytomegalovirus (HCMV) replication requires a metal‐dependent endonuclease at
the C‐terminus of pUL89 (pUL89‐C) for viral genome packaging and cleavage. We have …

Inhibition of human cytomegalovirus pUL89 terminase subunit blocks virus replication and genome cleavage

Y Wang, L Mao, J Kankanala, Z Wang… - Journal of …, 2017 - Am Soc Microbiol
The human cytomegalovirus terminase complex cleaves concatemeric genomic DNA into
unit lengths during genome packaging and particle assembly. This process is an attractive …

Mutual interplay between the human cytomegalovirus terminase subunits pUL51, pUL56, and pUL89 promotes terminase complex formation

S Neuber, K Wagner, T Goldner, P Lischka… - Journal of …, 2017 - Am Soc Microbiol
Human cytomegalovirus (HCMV) genome encapsidation requires several essential viral
proteins, among them pUL56, pUL89, and the recently described pUL51, which constitute …

[HTML][HTML] Identification of Small Molecule Inhibitors of Human Cytomegalovirus pUL89 Endonuclease Using Integrated Computational Approaches

M Almehmadi, IU Haq, AA Alsaiari, FM Alshabrmi… - Molecules, 2023 - mdpi.com
Replication of Human Cytomegalovirus (HCMV) requires the presence of a metal-
dependent endonuclease at the C-terminus of pUL89, in order to properly pack and cleave …